Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

HIV-1 Vif-derived peptide inhibits drug-resistant HIV proteases.

Biochemical and biophysical research communications - 12 Apr 2002

Blumenzweig Immanuel, Baraz Lea, Friedler Assaf, Danielson U Helena, Gilon Chaim, Steinitz Michael, Kotler Moshe

Abstract excerpt

Vif, one of the six accessory genes expressed by HIV-1, is essential for the productive infection of natural target cells. Previously we suggested that Vif acts as a regulator of the viral protease (PR): It prevents the autoprocessing of Gag and Gag-Pol precursors until virus assembly, and it may control the PR activity in the preintegration complex at the early stage of infection. It was demonstrated before that...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Aspartic Acid Endopeptidases
Share to Binding, Competitive

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Gene Products, vif

Share to HIV Protease

Share to HIV Protease Inhibitors

Share to vif Gene Products, Human Immunodeficiency Virus

Share to Viral Envelope Proteins

Source

Identifiers

PMID: 11944889
DOI: 10.1006/bbrc.2002.6732

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

HIV-1 Vif-derived peptide inhibits drug-resistant HIV proteases.PMID 11944889Read ↗

Intravirion processing of the human immunodeficiency virus type 1 Vif protein by the viral protease may be correlated with Vif function.Semantic proximity Read ↗

Cellular Targets of HIV-1 Protease: Just the Tip of the Iceberg?Semantic proximity Read ↗

Structural insights for HIV-1 therapeutic strategies targeting VifSemantic proximity Read ↗

Vpr14-88-Apobec3G fusion protein is efficiently incorporated into Vif-positive HIV-1 particles and inhibits viral infection.Semantic proximity Read ↗

Cellular Targets of the HIV-1 Protease: Just the Tip of the Iceberg?Semantic proximity Read ↗

Autocatalytic maturation, physical/chemical properties, and crystal structure of group N HIV-1 protease: relevance to drug resistance.Semantic proximity Read ↗

Amino Acid Insertions near Gag Cleavage Sites Restore the Otherwise Compromised Replication of Human Immunodeficiency Virus Type 1 Variants Resistant to Protease InhibitorsSemantic proximity Read ↗

Mutations in HIV-1 gag and pol compensate for the loss of viral fitness caused by a highly mutated protease.Semantic proximity Read ↗

Second locus involved in human immunodeficiency virus type 1 resistance to protease inhibitors.Semantic proximity Read ↗

Effect of sequence polymorphism and drug resistance on two HIV‐1 Gag processing sitesSemantic proximity Read ↗

Cell-dependent function of HIV-1 Vif for virus replication (Review).Semantic proximity Read ↗

An inhibitor of the protease blocks maturation of human and simian immunodeficiency viruses and spread of infection.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.